Dr James Birrell
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Email
james.birrell@essex.ac.uk -
Telephone
+44 (0) 1206 873370
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Location
Colchester Campus
Profile
Biography
James Birrell completed his PhD in 2012 at the MRC Mitochondrial Biology Unit and the University of Cambridge, UK, with Professor Judy Hirst FRS. He moved to Germany for postdoctoral work at the Max Planck Institute for Chemical Energy Conversion (MPI-CEC) with Professor Wolfgang Lubitz (2013–2017). He remained at MPI-CEC as a Group Leader in Professor Serena DeBeer's Bioinorganic Spectroscopy department (2017–2022). In 2022, James returned to the UK as a Lecturer at the University of Essex. James's present research interests are structural and functional aspects of anaerobic metabolism in bacteria and archaea.
Qualifications
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PhD: Bioscience University of Cambridge, (2012)
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BA/MSci: Natural Sciences: Biochemistry University of Cambridge, (2008)
Appointments
University of Essex
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Lecturer, School of Life Sciences, University of Essex (1/9/2022 - present)
Other academic
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Group Leader, Inorganic Spectroscopy, Max Planck Institute for Chemical Energy Conversion (3/7/2017 - 31/8/2022)
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Postdoc, Bioinorganic Chemistry, Max Planck Institute for Chemical Energy Conversion (2/9/2013 - 29/6/2017)
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Postdoc, Hirst Group, MRC Mitochondrial Biology Unit (1/10/2012 - 21/12/2012)
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PhD, Hirst Group, MRC Mitochondrial Biology Unit (1/10/2008 - 28/9/2012)
Research and professional activities
Research interests
[FeFe] hydrogenase structure and mechanism
[FeFe] hydrogenases are biological (enzyme) catalysts for the reversible interconversion of hydrogen with protons and electrons. They are extremely active and are of both fundamental scientific and biotechnological interest. They are found throughout nature where they allow microorganisms to use hydrogen as a source of energy and use protons as a terminal electron acceptor during fermentation. My group studies their active site as well as the protein environment in order to understand how the geometric and electronic structure are tuned for optimal catalytic performance. For this we use a variety of spectroscopic tools as well as state of the art structural biology methods, combined with electrochemistry and computational approaches.
Flavin-based electron-bifurcation
Electron-bifurcation is one of the three fundamental mechanisms of energetic coupling found in nature. By strictly coupling energetically favourable and unfavourable electron transfer processes, nature is able to drive challenging metabolic processes under anaerobic conditions such as methanogenesis and acetogenesis. The major class of electron-bifurcating enzymes use either flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) at for the coupling reaction as these molecules are capable of both two-electron and one-electron chemistry. However, the mechanism of electron-bifurcation is not yet understood. Insight into electron-bifurcation couple allow us to manipulate enzymes to enhance metabolic pathways or build new enzymes for biotechnological purposes. My group studies a particular class of electron-bifurcating enzymes with an FMN, which allows the bifurcation of electrons from electron donors such as hydrogen and carbon monoxide to the electron acceptors NAD+ and ferredoxin. We use a combination of cryoEM structure elucidation and spectroscopic approaches combined with site-directed mutagenesis to learn how these complicated electron-bifurcating enzymes function at the molecular level.
Biogeochemical cycling of hydrogen and carbon monoxide
Hydrogen is an extremely important gas for industry - it is used to produce fertilisers, refine steel and oil, and may be used as an energy storage medium for powering cars and heating homes. It is also a crucial electron-rich intermediate in many metabolic pathways of microorgansims particularly under anaerobic conditions. Carbon monoxide is a toxic gas to humans and many other organisms but serves as an essential source of electrons and carbon to many anaerobic bacteria and archaea. Meanwhile, CO is a crucial component of the Fischer-Tropsch process for producing hydrocarbons. Thus, if we want to make hydrocarbons from CO2 using green energy, understanding how enzymes deal with CO is of fundamental importance. My group studies how microorganisms utilise CO and H2 under anaerobic conditions as both sources of energy (reducing power) as well as for carbon fixation. We grow interesting bacteria and archaea in the lab as well as study their occupation of various natural environments. We purify enzyme complexes from these organisms to study their structure and function.
Conferences and presentations
Structural insights on the mechanism of the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima
Invited presentation, 21st European Bioenergetics Conference (EBEC), Aix-en-Provence, France, 21/8/2022
Structural insights on the mechanism of the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima
European Bioinorganic Chemistry Conference 2022, Saint-Martin-d'Hères, France, 20/7/2022
Structural insights on the mechanism of the electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima
International Conference for Solar Fuels 2021, 29/7/2021
The Catalytic Cycle of [FeFe] Hydrogenase: A Tale of Two Sites
Invited presentation, International Symposium for Applied Bioinorganic Chemistry 2019, Nara, Japan, 3/6/2019
The Catalytic Cycle of [FeFe] Hydrogenase: A Tale of Two Sites
Keynote presentation, GRC Metals in Biology, Four Points Sheraton / Holiday Inn Express, Ventura, United States, 21/1/2018
Teaching and supervision
Current teaching responsibilities
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Employability Skills for the Biosciences (BS211)
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Metals in Biotechnology (BS228)
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Protein Bioinformatics (BS281)
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Industrial Biotechnology (BS937)
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Protein Technologies and Proteomics (BS983)
Publications
Publications (2)
Martini, MA., Bikbaev, K., Pang, Y., Lorent, C., Wiemann, C., Breuer, N., Zebger, I., DeBeer, S., Span, I., Bjornsson, R., Birrell, JA. and Rodriguez Macia, P., (2022). Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases
Folgosa, F., Pelmenschikov, V., Keck, M., Lorent, C., Yoda, Y., Birrell, JA., Kaupp, M., Teixeira, M., Tamasaku, K., Limberg, C. and Lauterbach, L., (2020). Hydroxo-Bridged Active Site of Flavodiiron NO Reductase Revealed by Spectroscopy and Computations
Journal articles (53)
Fasano, A., Baffert, C., Schumann, C., Berggren, G., Birrell, JA., Fourmond, V. and Léger, C., (2024). Kinetic Modeling of the Reversible or Irreversible Electrochemical Responses of FeFe-Hydrogenases.. Journal of the American Chemical Society. 146 (2), 1455-1466
Takeda, K., Birrell, JA., Kusuoka, R., Minami, T., Igarashi, K. and Nakamura, N., (2024). Redox Properties of Pyrroloquinoline Quinone in Pyranose Dehydrogenase Measured by Direct Electron Transfer. ACS Catalysis. 14 (16), 12242-12250
Lachmann, MT., Duan, Z., Rodríguez-Maciá, P. and Birrell, JA., (2024). The missing pieces in the catalytic cycle of [FeFe] hydrogenases. Chemical Science. 15 (35), 14062-14080
Martini, MA., Bikbaev, K., Pang, Y., Lorent, C., Wiemann, C., Breuer, N., Zebger, I., DeBeer, S., Span, I., Bjornsson, R., Birrell, JA. and Rodríguez-Maciá, P., (2023). Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases. Chemical Science. 14 (11), 2826-2838
Chongdar, N., Rodríguez-Maciá, P., Reijerse, EJ., Lubitz, W., Ogata, H. and Birrell, JA., (2023). Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from Thermotoga maritima. Chemical Science. 14 (13), 3682-3692
Lorenzi, M., Ceccaldi, P., Rodríguez-Maciá, P., Redman, HJ., Zamader, A., Birrell, JA., Mészáros, LS. and Berggren, G., (2022). Stability of the H-cluster under whole-cell conditions-formation of an Htrans-like state and its reactivity towards oxygen.. Journal of Biological Inorganic Chemistry. 27 (3), 345-355
Sanchez, MLK., Wiley, S., Reijerse, E., Lubitz, W., Birrell, JA. and Dyer, RB., (2022). Time-Resolved Infrared Spectroscopy Reveals the pH-Independence of the First Electron Transfer Step in the [FeFe] Hydrogenase Catalytic Cycle.. Journal of Physical Chemistry Letters. 13 (25), 5986-5990
Chatterjee, S., Harden, I., Bistoni, G., Castillo, RG., Chabbra, S., van Gastel, M., Schnegg, A., Bill, E., Birrell, JA., Morandi, B., Neese, F. and DeBeer, S., (2022). A Combined Spectroscopic and Computational Study on the Mechanism of Iron-Catalyzed Aminofunctionalization of Olefins Using Hydroxylamine Derived N-O Reagent as the "Amino" Source and "Oxidant".. Journal of the American Chemical Society. 144 (6), 2637-2656
Furlan, C., Chongdar, N., Gupta, P., Lubitz, W., Ogata, H., Blaza, JN. and Birrell, JA., (2022). Structural insight on the mechanism of an electron-bifurcating [FeFe] hydrogenase.. eLife. 11, e79361-
Becker, JM., Lielpetere, A., Szczesny, J., Junqueira, JRC., Rodríguez-Maciá, P., Birrell, JA., Conzuelo, F. and Schuhmann, W., (2022). Bioelectrocatalytic CO₂ Reduction by Redox Polymer-Wired Carbon Monoxide Dehydrogenase Gas Diffusion Electrodes. ACS Applied Materials and Interfaces. 14 (41), 46421-46426
Lielpetere, A., Becker, JM., Szczesny, J., Conzuelo, F., Ruff, A., Birrell, J., Lubitz, W. and Schuhmann, W., (2022). Enhancing the catalytic current response of H2 oxidation gas diffusion bioelectrodes using an optimized viologen‐based redox polymer and [NiFe] hydrogenase. Electrochemical Science Advances. 2 (4)
Pelmenschikov, V., Birrell, JA., Gee, LB., Richers, CP., Reijerse, EJ., Wang, H., Arragain, S., Mishra, N., Yoda, Y., Matsuura, H., Li, L., Tamasaku, K., Rauchfuss, TB., Lubitz, W. and Cramer, SP., (2021). Vibrational Perturbation of the [FeFe] Hydrogenase H-Cluster Revealed by 13C2H-ADT Labeling. Journal of the American Chemical Society. 143 (22), 8237-8243
Birrell, JA., Rodríguez-Maciá, P., Reijerse, EJ., Martini, MA. and Lubitz, W., (2021). The catalytic cycle of [FeFe] hydrogenase: A tale of two sites. Coordination Chemistry Reviews. 449, 214191-214191
Birrell, JA., Rodríguez-Maciá, P. and Hery-Barranco, A., (2021). A Beginner’s Guide to Thermodynamic Modelling of [FeFe] Hydrogenase. Catalysts. 11 (2), 238-238
Hardt, S., Stapf, S., Filmon, DT., Birrell, JA., Rüdiger, O., Fourmond, V., Léger, C. and Plumeré, N., (2021). Reversible H₂ Oxidation and Evolution by Hydrogenase Embedded in a Redox Polymer Film.. Nature Catalysis. 4 (3), 251-258
Rosenbach, H., Walla, E., Cutsail, GE., Birrell, JA., Pascual-Ortiz, M., DeBeer, S., Fleig, U. and Span, I., (2021). The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]²⁺ cluster in vivo.. Journal of Biological Inorganic Chemistry. 26 (1), 93-108
Martini, MA., Rüdiger, O., Breuer, N., Nöring, B., DeBeer, S., Rodríguez-Maciá, P. and Birrell, JA., (2021). The Nonphysiological Reductant Sodium Dithionite and [FeFe] Hydrogenase: Influence on the Enzyme Mechanism.. Journal of the American Chemical Society. 143 (43), 18159-18171
Takeda, K., Kusuoka, R., Birrell, JA., Yoshida, M., Igarashi, K. and Nakamura, N., (2020). Bioelectrocatalysis based on direct electron transfer of fungal pyrroloquinoline quinone-dependent dehydrogenase lacking the cytochrome domain. Electrochimica Acta. 359, 136982-136982
Szczesny, J., Birrell, JA., Conzuelo, F., Lubitz, W., Ruff, A. and Schuhmann, W., (2020). Redox‐Polymer‐Based High‐Current‐Density Gas‐Diffusion H2‐Oxidation Bioanode Using [FeFe] Hydrogenase from Desulfovibrio desulfuricans in a Membrane‐free Biofuel Cell. Angewandte Chemie International Edition. 59 (38), 16506-16510
Rodríguez-Maciá, P., Breuer, N., DeBeer, S. and Birrell, JA., (2020). Insight into the Redox Behavior of the [4Fe–4S] Subcluster in [FeFe] Hydrogenases. ACS Catalysis. 10 (21), 13084-13095
Birrell, JA., Pelmenschikov, V., Mishra, N., Wang, H., Yoda, Y., Tamasaku, K., Rauchfuss, TB., Cramer, SP., Lubitz, W. and DeBeer, S., (2020). Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates. Journal of the American Chemical Society. 142 (1), 222-232
Van Stappen, C., Decamps, L., Cutsail, GE., Bjornsson, R., Henthorn, JT., Birrell, JA. and DeBeer, S., (2020). The Spectroscopy of Nitrogenases. Chemical Reviews. 120 (12), 5005-5081
Oughli, AA., Hardt, S., Rüdiger, O., Birrell, JA. and Plumeré, N., (2020). Reactivation of sulfide-protected [FeFe] hydrogenase in a redox-active hydrogel. Chemical Communications. 56 (69), 9958-9961
Jagilinki, BP., Ilic, S., Trncik, C., Tyryshkin, AM., Pike, DH., Lubitz, W., Bill, E., Einsle, O., Birrell, JA., Akabayov, B., Noy, D. and Nanda, V., (2020). In Vivo Biogenesis of a De Novo Designed Iron–Sulfur Protein. ACS Synthetic Biology. 9 (12), 3400-3407
Reijerse, E., Birrell, JA. and Lubitz, W., (2020). Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State. The Journal of Physical Chemistry Letters. 11 (12), 4597-4602
Sanchez, MLK., Konecny, SE., Narehood, SM., Reijerse, EJ., Lubitz, W., Birrell, JA. and Dyer, RB., (2020). The Laser-Induced Potential Jump: A Method for Rapid Electron Injection into Oxidoreductase Enzymes. The Journal of Physical Chemistry B. 124 (40), 8750-8760
Rodríguez‐Maciá, P., Galle, LM., Bjornsson, R., Lorent, C., Zebger, I., Yoda, Y., Cramer, SP., DeBeer, S., Span, I. and Birrell, JA., (2020). Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2‐stable State of [FeFe] Hydrogenase. Angewandte Chemie International Edition. 59 (38), 16786-16794
Chongdar, N., Pawlak, K., Rüdiger, O., Reijerse, EJ., Rodríguez-Maciá, P., Lubitz, W., Birrell, JA. and Ogata, H., (2020). Spectroscopic and biochemical insight into an electron-bifurcating [FeFe] hydrogenase. JBIC Journal of Biological Inorganic Chemistry. 25 (1), 135-149
Reijerse, EJ., Pelmenschikov, V., Birrell, JA., Richers, CP., Kaupp, M., Rauchfuss, TB., Cramer, SP. and Lubitz, W., (2019). Asymmetry in the Ligand Coordination Sphere of the [FeFe] Hydrogenase Active Site Is Reflected in the Magnetic Spin Interactions of the Aza-propanedithiolate Ligand. The Journal of Physical Chemistry Letters. 10 (21), 6794-6799
Sanchez, MLK., Sommer, C., Reijerse, E., Birrell, JA., Lubitz, W. and Dyer, RB., (2019). Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-Resolved Infrared Spectroscopy. Journal of the American Chemical Society. 141 (40), 16064-16070
Rodríguez-Maciá, P., Kertess, L., Burnik, J., Birrell, JA., Hofmann, E., Lubitz, W., Happe, T. and Rüdiger, O., (2019). His-Ligation to the [4Fe–4S] Subcluster Tunes the Catalytic Bias of [FeFe] Hydrogenase. Journal of the American Chemical Society. 141 (1), 472-481
Schuller, JM., Birrell, JA., Tanaka, H., Konuma, T., Wulfhorst, H., Cox, N., Schuller, SK., Thiemann, J., Lubitz, W., Sétif, P., Ikegami, T., Engel, BD., Kurisu, G. and Nowaczyk, MM., (2019). Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science. 363 (6424), 257-260
Rodríguez-Maciá, P., Reijerse, EJ., van Gastel, M., DeBeer, S., Lubitz, W., Rüdiger, O. and Birrell, JA., (2018). Sulfide Protects [FeFe] Hydrogenases From O2. Journal of the American Chemical Society. 140 (30), 9346-9350
Oughli, AA., Vélez, M., Birrell, JA., Schuhmann, W., Lubitz, W., Plumeré, N. and Rüdiger, O., (2018). Viologen-modified electrodes for protection of hydrogenases from high potential inactivation while performing H2oxidation at low overpotential. Dalton Transactions. 47 (31), 10685-10691
Chongdar, N., Birrell, JA., Pawlak, K., Sommer, C., Reijerse, EJ., Rüdiger, O., Lubitz, W. and Ogata, H., (2018). Unique Spectroscopic Properties of the H-Cluster in a Putative Sensory [FeFe] Hydrogenase. Journal of the American Chemical Society. 140 (3), 1057-1068
Rodríguez‐Maciá, P., Birrell, JA., Lubitz, W. and Rüdiger, O., (2017). Electrochemical Investigations on the Inactivation of the [FeFe] Hydrogenase from Desulfovibrio desulfuricans by O2 or Light under Hydrogen‐Producing Conditions. ChemPlusChem. 82 (4), 540-545
Birrell, JA., Rüdiger, O., Reijerse, EJ. and Lubitz, W., (2017). Semisynthetic Hydrogenases Propel Biological Energy Research into a New Era. Joule. 1 (1), 61-76
Pelmenschikov, V., Birrell, JA., Pham, CC., Mishra, N., Wang, H., Sommer, C., Reijerse, E., Richers, CP., Tamasaku, K., Yoda, Y., Rauchfuss, TB., Lubitz, W. and Cramer, SP., (2017). Reaction Coordinate Leading to H2 Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory. Journal of the American Chemical Society. 139 (46), 16894-16902
Rodríguez-Maciá, P., Pawlak, K., Rüdiger, O., Reijerse, EJ., Lubitz, W. and Birrell, JA., (2017). Intercluster Redox Coupling Influences Protonation at the H-cluster in [FeFe] Hydrogenases. Journal of the American Chemical Society. 139 (42), 15122-15134
Rodríguez-Maciá, P., Reijerse, E., Lubitz, W., Birrell, JA. and Rüdiger, O., (2017). Spectroscopic Evidence of Reversible Disassembly of the [FeFe] Hydrogenase Active Site. The Journal of Physical Chemistry Letters. 8 (16), 3834-3839
Sommer, C., Adamska-Venkatesh, A., Pawlak, K., Birrell, JA., Rüdiger, O., Reijerse, EJ. and Lubitz, W., (2017). Proton Coupled Electronic Rearrangement within the H-Cluster as an Essential Step in the Catalytic Cycle of [FeFe] Hydrogenases. Journal of the American Chemical Society. 139 (4), 1440-1443
Birrell, JA., Laurich, C., Reijerse, EJ., Ogata, H. and Lubitz, W., (2016). Importance of Hydrogen Bonding in Fine Tuning the [2Fe-2S] Cluster Redox Potential of HydC from Thermotoga maritima. Biochemistry. 55 (31), 4344-4355
Birrell, JA., Wrede, K., Pawlak, K., Rodriguez‐Maciá, P., Rüdiger, O., Reijerse, EJ. and Lubitz, W., (2016). Artificial Maturation of the Highly Active Heterodimeric [FeFe] Hydrogenase from Desulfovibrio desulfuricans ATCC 7757. Israel Journal of Chemistry. 56 (9-10), 852-863
Kutin, Y., Srinivas, V., Fritz, M., Kositzki, R., Shafaat, HS., Birrell, J., Bill, E., Haumann, M., Lubitz, W., Högbom, M., Griese, JJ. and Cox, N., (2016). Divergent assembly mechanisms of the manganese/iron cofactors in R2lox and R2c proteins. Journal of Inorganic Biochemistry. 162, 164-177
Fourmond, V., Stapf, S., Li, H., Buesen, D., Birrell, J., Rüdiger, O., Lubitz, W., Schuhmann, W., Plumeré, N. and Léger, C., (2015). Mechanism of Protection of Catalysts Supported in Redox Hydrogel Films. Journal of the American Chemical Society. 137 (16), 5494-5505
Birrell, JA., Morina, K., Bridges, HR., Friedrich, T. and Hirst, J., (2013). Investigating the function of [2Fe–2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential. Biochemical Journal. 456 (1), 139-146
Birrell, JA. and Hirst, J., (2013). Investigation of NADH Binding, Hydride Transfer, and NAD+ Dissociation during NADH Oxidation by Mitochondrial Complex I Using Modified Nicotinamide Nucleotides. Biochemistry. 52 (23), 4048-4055
Birrell, JA. and Jacobsen, EN., (2013). A Practical Method for the Synthesis of Highly Enantioenriched trans-1,2-Amino Alcohols. Organic Letters. 15 (12), 2895-2897
Birrell, JA., King, MS. and Hirst, J., (2011). A ternary mechanism for NADH oxidation by positively charged electron acceptors, catalyzed at the flavin site in respiratory complex I. FEBS Letters. 585 (14), 2318-2322
Bridges, HR., Birrell, JA. and Hirst, J., (2011). The mitochondrial-encoded subunits of respiratory complex I (NADH:ubiquinone oxidoreductase): identifying residues important in mechanism and disease. Biochemical Society Transactions. 39 (3), 799-806
Birrell, JA., Desrosiers, J-N. and Jacobsen, EN., (2011). Enantioselective Acylation of Silyl Ketene Acetals through Fluoride Anion-Binding Catalysis. Journal of the American Chemical Society. 133 (35), 13872-13875
Birrell, JA. and Hirst, J., (2010). Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter‐like subunits in complex I from higher metazoans. FEBS Letters. 584 (19), 4247-4252
Birrell, JA., Yakovlev, G. and Hirst, J., (2009). Reactions of the Flavin Mononucleotide in Complex I: A Combined Mechanism Describes NADH Oxidation Coupled to the Reduction of APAD+, Ferricyanide, or Molecular Oxygen. Biochemistry. 48 (50), 12005-12013
Book chapters (1)
Cox, N., Birrell, JA. and Lubitz, W., (2022). 8 Molecular Concepts of Water Splitting and Hydrogen Production: Nature’s Approach. In: Chemical Energy Storage. De Gruyter. 183- 242
Conferences (1)
Zuchan, K., Breuer, N., Laurich, C., Nitschke, W., Birrell, J. and Baymann, F., (2024). Thermodynamic landscape of the redox-centers in the electron-confurcating [FeFe]-Hydrogenase (HydABC) of Thermotoga maritima
Grants and funding
2024
Summer Vacation Studentship 2024 (Tif Allamki)
Biochemical Society
2023
TRICSS - a multi-user high-throughput platform to quantify biological interactions in solution
Biotechnology and Biological Sciences Research Council
Toward sustainable energy storage: production and characterisation of an electron-bifurcating CO dehydrogenase
Royal Society of Chemistry
Toward sustainable energy storage: deciphering the mechanism of an electron-bifurcating CO dehydrogenase via electron cryomicroscopy
The Royal Society
TRICSS - a multi-user high-throughput platform to quantify biological interactions in solution
Biotechnology and Biological Sciences Research Council
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